排序方式: 共有95条查询结果,搜索用时 15 毫秒
91.
92.
Khadija Mohamed Ahmad Olena P. Ishchuk Linda Hellborg Gloria Jørgensen Miha Skvarc Jørgen Stenderup Dorte Jørck-Ramberg Silvia Polakova Jure Piškur 《Antonie van Leeuwenhoek》2013,104(1):111-122
We analyzed 192 strains of the pathogenic yeast Candida glabrata from patients, mainly suffering from systemic infection, at Danish hospitals during 1985–1999. Our analysis showed that these strains were closely related but exhibited large karyotype polymorphism. Nine strains contained small chromosomes, which were smaller than 0.5 Mb. Regarding the year, patient and hospital, these C. glabrata strains had independent origin and the analyzed small chromosomes were structurally not related to each other (i.e. they contained different sets of genes). We suggest that at least two mechanisms could participate in their origin: (i) through a segmental duplication which covered the centromeric region, or (ii) by a translocation event moving a larger chromosome arm to another chromosome that leaves the centromere part with the shorter arm. The first type of small chromosomes carrying duplicated genes exhibited mitotic instability, while the second type, which contained the corresponding genes in only one copy in the genome, was mitotically stable. Apparently, in patients C. glabrata chromosomes are frequently reshuffled resulting in new genetic configurations, including appearance of small chromosomes, and some of these resulting “mutant” strains can have increased fitness in a certain patient “environment”. 相似文献
93.
94.
Miha Črnigoj Rok Kostanjšek Gönül Kaletunç Nataša Poklar Ulrih 《World journal of microbiology & biotechnology》2008,24(10):2115-2123
The interactions of DNA-binding dyes (Hoechst 33258, DAPI, acridine orange) and DiBAC4(3) with hyperthermophilic archaeon Aeropyrum pernix cells were investigated by the combination of calorimetric, spectroscopic and microscopic techniques. All of the dyes, studied
here, affect the thermal stability of DNA in vivo and in vitro. Hoechst 33258 is highly DNA-specific probe, which does not
affect the thermal transitions of other cellular components as can be detected by differential scanning calorimetry (DSC).
Due to this unique property, it can be used as a potential DNA marker for in vivo DSC studies. The localization of the dyes
in the cells and viability assay was revealed by fluorescence microscopy. Hoechst 33258, DAPI and acridine orange did not
distinguish between viable and non-viable cells of Aeropyrum pernix. Only with the commercially available Live/Dead BacLightTM kit we were able to discriminate viable and non-viable Aeropyrum pernix cells. 相似文献
95.
Julius Kostan Miha Pavi
Vid Pu Thomas C. Schwarz Friedel Drepper Sibylle Molt Melissa Ann Graewert Claudia Schreiner Sara Sajko Peter F. M. van der Ven Adekunle Onipe Dmitri I. Svergun Bettina Warscheid Robert Konrat Dieter O. Fürst Brigita Lenar
i
Kristina Djinovi-Carugo 《PLoS biology》2021,19(4)
Sarcomeres, the basic contractile units of striated muscle cells, contain arrays of thin (actin) and thick (myosin) filaments that slide past each other during contraction. The Ig-like domain-containing protein myotilin provides structural integrity to Z-discs—the boundaries between adjacent sarcomeres. Myotilin binds to Z-disc components, including F-actin and α-actinin-2, but the molecular mechanism of binding and implications of these interactions on Z-disc integrity are still elusive. To illuminate them, we used a combination of small-angle X-ray scattering, cross-linking mass spectrometry, and biochemical and molecular biophysics approaches. We discovered that myotilin displays conformational ensembles in solution. We generated a structural model of the F-actin:myotilin complex that revealed how myotilin interacts with and stabilizes F-actin via its Ig-like domains and flanking regions. Mutant myotilin designed with impaired F-actin binding showed increased dynamics in cells. Structural analyses and competition assays uncovered that myotilin displaces tropomyosin from F-actin. Our findings suggest a novel role of myotilin as a co-organizer of Z-disc assembly and advance our mechanistic understanding of myotilin’s structural role in Z-discs.Myotilin is a scaffold protein in the Z-disc, the boundary between adjacent sarcomeres, aiding structural integrity via multiple interactions, including F-actin and α-actinin-2. An integrative structural model of the complex between myotilin and F-actin reveals that myotilin displaces tropomyosin from F-actin, implying a novel role of myotilin in sarcomere biogenesis beyond a mere interaction hub. 相似文献